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Literature summary for 3.1.4.37 extracted from

  • Rao, F.; Qi, Y.; Murugan, E.; Pasunooti, S.; Ji, Q.
    2',3'-cAMP hydrolysis by metal-dependent phosphodiesterases containing DHH, EAL, and HD domains is non-specific: implications for PDE screening (2010), Biochem. Biophys. Res. Commun., 398, 500-505.
    View publication on PubMed
Search for more literature for 3.1.4.37

Inhibitors

Inhibitors Comment Organism Structure
EDTA
-
 Rattus norvegicus

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ activates Rattus norvegicus
Mn2+ activates Rattus norvegicus

Organism

Organism UniProt Comment Textmining
Rattus norvegicus
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
kidney
-
 Rattus norvegicus
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2',3'-cAMP + H2O the exclusive formation of 3'-AMP is due to the P-O2' bond having lower activation energy and is not the result of steric exclusion at enzyme active site, kinetic evidence that hydrolysis of 2',3'-cAMP into 3'-AMP is nonspecific. Modeling of 2',3'-cyclic nucleotide into the active site of a EAL domain PDE, overview Rattus norvegicus 3'-AMP + ?
-
 ?
bis(p-nitrophenyl)phosphate + H2O non-specific substrate Rattus norvegicus ?
-
 ?
additional information substrate specificities and activities of RocR, DGC2, YybT, YtqI, 3DMA, and PaAcpH with 2',3'-cAMP, overview Rattus norvegicus ?
-
 ?

Synonyms

Synonyms Comment Organism
3DMA
-
 Rattus norvegicus
DGC2
-
 Rattus norvegicus
PaAcpH
-
 Rattus norvegicus
RocR
-
 Rattus norvegicus
YtqI
-
 Rattus norvegicus
YybT
-
 Rattus norvegicus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8 8.3 assay at Rattus norvegicus